ID A0A0C1L236_9BACT Unreviewed; 398 AA.
AC A0A0C1L236;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Cytochrome C peroxidase {ECO:0000313|EMBL:KIC94042.1};
GN ORFNames=OI18_13615 {ECO:0000313|EMBL:KIC94042.1};
OS Flavihumibacter solisilvae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1349421 {ECO:0000313|EMBL:KIC94042.1, ECO:0000313|Proteomes:UP000031408};
RN [1] {ECO:0000313|EMBL:KIC94042.1, ECO:0000313|Proteomes:UP000031408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-3 {ECO:0000313|EMBL:KIC94042.1,
RC ECO:0000313|Proteomes:UP000031408};
RA Zhou G., Li M., Wang G.;
RT "Genome sequence of Flavihumibacter solisilvae 3-3.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR000294-1};
CC Note=Binds 2 heme groups. {ECO:0000256|PIRSR:PIRSR000294-1};
CC -!- PTM: Binds 2 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000294-
CC 1}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIC94042.1}.
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DR EMBL; JSVC01000015; KIC94042.1; -; Genomic_DNA.
DR RefSeq; WP_039140583.1; NZ_JSVC01000015.1.
DR AlphaFoldDB; A0A0C1L236; -.
DR STRING; 1349421.OI18_13615; -.
DR OrthoDB; 9805202at2; -.
DR Proteomes; UP000031408; Unassembled WGS sequence.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR InterPro; IPR026259; MauG/Cytc_peroxidase.
DR PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR Pfam; PF03150; CCP_MauG; 1.
DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|PIRSR:PIRSR000294-1};
KW Iron {ECO:0000256|PIRSR:PIRSR000294-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000294-2};
KW Oxidoreductase {ECO:0000313|EMBL:KIC94042.1};
KW Peroxidase {ECO:0000313|EMBL:KIC94042.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031408}.
FT DOMAIN 63..245
FT /note="Di-haem cytochrome c peroxidase"
FT /evidence="ECO:0000259|Pfam:PF03150"
FT REGION 27..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 88
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 89
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
FT BINDING 264
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 267
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 268
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
SQ SEQUENCE 398 AA; 44157 MW; 48424AC37F071EAD CRC64;
MRLKVIVILV ALIVSCLVMV ESCKSPADER KPAHRRKEQV DPGKISALPE TFESPAGNPT
TAQKIELGRL LFYDPVLSGG NDVACATCHH PEFGYAESLQ LSIGVNGRGL GEQRHFNSRN
KIPFTKRNAQ SLLNVAFSGI DQEGNYIPAE APMFWDLRAG GLEEQAMMPV RTLEEMRGHG
YGEEDITNEV AKRVGKIATY RKLFKSAFGT DEAVSVENIS KALASFQRSL VANNSRFDRY
MRGDKTAMSA REIEGMQLFI SSGCARCHSG PMLSDYKTHV LGVAESELLS LPDSGFMKSF
AFRTPTLRNL RFTRPYMHNG KIQTLNDVLT FYEDLPGKDL PNPHVKKEQL DTLAGMVKVK
FGDINTIVEF LNTLNDEKYD RKIPESVPSG LPVGGNIH
//
